5MAT_ARATH
ID 5MAT_ARATH Reviewed; 449 AA.
AC Q9LJB4;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Malonyl-CoA:anthocyanidin 5-O-glucoside-6''-O-malonyltransferase;
DE EC=2.3.1.-;
DE AltName: Full=Anthocyanin 5-aromatic acyltransferase-like protein;
DE Short=At5MAT;
GN Name=5MAT; OrderedLocusNames=At3g29590; ORFNames=MTO24.5;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=17292360; DOI=10.1016/j.febslet.2007.01.060;
RA D'Auria J.C., Reichelt M., Luck K., Svatos A., Gershenzon J.;
RT "Identification and characterization of the BAHD acyltransferase malonyl
RT CoA: anthocyanidin 5-O-glucoside-6''-O-malonyltransferase (At5MAT) in
RT Arabidopsis thaliana.";
RL FEBS Lett. 581:872-878(2007).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION
RP PHENOTYPE, INDUCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=17425720; DOI=10.1111/j.1365-313x.2007.03079.x;
RA Luo J., Nishiyama Y., Fuell C., Taguchi G., Elliott K., Hill L., Tanaka Y.,
RA Kitayama M., Yamazaki M., Bailey P., Parr A., Michael A.J., Saito K.,
RA Martin C.;
RT "Convergent evolution in the BAHD family of acyl transferases:
RT identification and characterization of anthocyanin acyl transferases from
RT Arabidopsis thaliana.";
RL Plant J. 50:678-695(2007).
RN [5]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=23473981; DOI=10.1016/j.plaphy.2013.02.001;
RA Saito K., Yonekura-Sakakibara K., Nakabayashi R., Higashi Y., Yamazaki M.,
RA Tohge T., Fernie A.R.;
RT "The flavonoid biosynthetic pathway in Arabidopsis: Structural and genetic
RT diversity.";
RL Plant Physiol. Biochem. 72:21-34(2013).
CC -!- FUNCTION: Involved in the malonylation of the 5-O-glucose residue of
CC anthocyanin. Acts only on anthocyanin substrates containing a 5-O
CC glucosyl moiety. Not able to catalyze acyl transfer using acetyl-CoA,
CC butyryl-CoA, hexanoyl- CoA, benzoyl-CoA, cinnamoyl-CoA, methylmalonyl-
CC CoA, succinyl-CoA, p-coumaroyl-CoA or caffeoyl-CoA.
CC {ECO:0000269|PubMed:17292360, ECO:0000269|PubMed:17425720}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=167 uM for cyanin {ECO:0000269|PubMed:17292360,
CC ECO:0000269|PubMed:17425720};
CC KM=2260 uM for malvin {ECO:0000269|PubMed:17292360,
CC ECO:0000269|PubMed:17425720};
CC KM=70 uM for cyanidin 3-O-[2''-O-(xylosyl)-6''-O-(p-O-(glucosyl)-p-
CC coumaroyl) glucoside]5-O-glucoside {ECO:0000269|PubMed:17292360,
CC ECO:0000269|PubMed:17425720};
CC KM=7.6 uM for cyanidin 3-O-[2''-O-(2'''-O-(sinapoyl) xylosyl)6''-O-
CC (p-O-(glucosyl) p-coumaroyl) glucoside]5-O-glucoside
CC {ECO:0000269|PubMed:17292360, ECO:0000269|PubMed:17425720};
CC KM=6.6 uM for cyanidin 3,5-diglucoside {ECO:0000269|PubMed:17292360,
CC ECO:0000269|PubMed:17425720};
CC KM=4.5 uM for pelargonidine 3,5-diglucoside
CC {ECO:0000269|PubMed:17292360, ECO:0000269|PubMed:17425720};
CC KM=6.9 uM for peonidine 3,5-diglucoside {ECO:0000269|PubMed:17292360,
CC ECO:0000269|PubMed:17425720};
CC KM=15.3 uM for malonyl-CoA (with cyanidin 3-O-[2''-O-(xylosyl)-6''-O-
CC (p-O-(glucosyl)-p-coumaroyl) glucoside]5-O-glucoside as cosubstrate)
CC {ECO:0000269|PubMed:17292360, ECO:0000269|PubMed:17425720};
CC KM=2.1 uM for malonyl-CoA (with cyanidin 3-O-[2''-O-(2'''-O-
CC (sinapoyl) xylosyl)6''-O-(p-O-(glucosyl) p-coumaroyl) glucoside]5-O-
CC glucoside as cosubstrate) {ECO:0000269|PubMed:17292360,
CC ECO:0000269|PubMed:17425720};
CC KM=5.5 uM for malonyl-CoA (with cyanidin 3,5-diglucoside as
CC cosubstrate) {ECO:0000269|PubMed:17292360,
CC ECO:0000269|PubMed:17425720};
CC Note=kcat is 0.02 sec(-1) for cyanin. kcat is 1.79 sec(-1) for
CC malvin. kcat is 0.12 sec(-1) for cyanidin 3-O-[2''-O-(xylosyl)-6''-O-
CC (p-O-(glucosyl)-p-coumaroyl) glucoside]5-O-glucoside. kcat is 0.00012
CC sec(-1) for cyanidin 3-O-[2''-O-(2'''-O-(sinapoyl) xylosyl)6''-O-(p-
CC O-(glucosyl) p-coumaroyl) glucoside]5-O-glucosid. kcat is 6.4 sec(-1)
CC for cyanidin 3,5-diglucoside. kcat is 5.9 sec(-1) for pelargonidine
CC 3,5-diglucoside. kcat is 6.6 sec(-1) for peonidine 3,5-diglucoside.
CC kcat is 0.2 sec(-1) for malonyl-CoA (with cyanidin 3-O-[2''-O-
CC (xylosyl)-6''-O-(p-O-(glucosyl)-p-coumaroyl) glucoside]5-O-glucoside
CC as cosubstrate). kcat is 0.0013 sec(-1) for malonyl-CoA (with
CC cyanidin 3-O-[2''-O-(2'''-O-(sinapoyl) xylosyl)6''-O-(p-O-(glucosyl)
CC p-coumaroyl) glucoside]5-O-glucoside as cosubstrate). kcat is 6.4
CC sec(-1) for malonyl-CoA (with cyanidin 3,5-diglucoside as
CC cosubstrate).;
CC pH dependence:
CC Optimum pH is 6.0-7.5. {ECO:0000269|PubMed:17292360,
CC ECO:0000269|PubMed:17425720};
CC -!- TISSUE SPECIFICITY: Expressed in flowers. Detected in leaves, stems,
CC roots and siliques. {ECO:0000269|PubMed:17425720}.
CC -!- INDUCTION: Up-regulated by high sucrose and by low phosphate stresses.
CC {ECO:0000269|PubMed:17425720}.
CC -!- DISRUPTION PHENOTYPE: Absence of malonyl-modified anthocyanins.
CC {ECO:0000269|PubMed:17292360, ECO:0000269|PubMed:17425720}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
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DR EMBL; AP000606; BAB01191.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77592.1; -; Genomic_DNA.
DR RefSeq; NP_189600.1; NM_113880.2.
DR AlphaFoldDB; Q9LJB4; -.
DR SMR; Q9LJB4; -.
DR STRING; 3702.AT3G29590.1; -.
DR PaxDb; Q9LJB4; -.
DR PRIDE; Q9LJB4; -.
DR ProteomicsDB; 244555; -.
DR DNASU; 822623; -.
DR EnsemblPlants; AT3G29590.1; AT3G29590.1; AT3G29590.
DR GeneID; 822623; -.
DR Gramene; AT3G29590.1; AT3G29590.1; AT3G29590.
DR KEGG; ath:AT3G29590; -.
DR Araport; AT3G29590; -.
DR TAIR; locus:2093620; AT3G29590.
DR eggNOG; ENOG502QPXT; Eukaryota.
DR HOGENOM; CLU_014546_7_0_1; -.
DR OMA; RTATEFH; -.
DR OrthoDB; 1130893at2759; -.
DR PhylomeDB; Q9LJB4; -.
DR BioCyc; ARA:AT3G29590-MON; -.
DR BioCyc; MetaCyc:MON-18509; -.
DR BRENDA; 2.3.1.172; 399.
DR PRO; PR:Q9LJB4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LJB4; baseline and differential.
DR Genevisible; Q9LJB4; AT.
DR GO; GO:0050736; F:O-malonyltransferase activity; IDA:TAIR.
DR GO; GO:0009718; P:anthocyanin-containing compound biosynthetic process; IDA:TAIR.
DR Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR023213; CAT-like_dom_sf.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..449
FT /note="Malonyl-CoA:anthocyanidin 5-O-glucoside-6''-O-
FT malonyltransferase"
FT /id="PRO_0000419539"
FT ACT_SITE 162
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 394
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q940Z5"
SQ SEQUENCE 449 AA; 49440 MW; 2446D502AEC9D99B CRC64;
MVNFNSAVNI LEVVQVSPPS SNSLTLPLTY FDLGWLKLHP VDRVLFYHVP ELTRSSLISK
LKSSLSATLL HYLPLAGRLV WDSIKTKPSI VYSPDDKDAV YLTVAESNGD LSHLSGDEPR
PATEFHSLVP ELPVSDESAR VLAVQVTFFP NQGFSLGVTA HHAVLDGKTT AMFLKAWAHN
CKQEQEALPH DLVPSLDRII VQDPTGLETK LLNRWISASN NKPSLKLFPS KIIGSDILRV
TYRLTREDIK KLRERVETES HAKQLRLSTF VITYAYVITC MVKMRGGDPT RFVCVGFASD
FRSRLNPPLP PTFFGNCIVG SGDFDVKAEP ILEEGEGKGF ITAVETLTGW VNGLCPENIE
KNMLLPFEAF KRMEPGRQMI SVAGSTRLGI YGSDFGWGKP VKVEIVTIDK DASVSLSESG
DGSGGVEVGV CLKKDDVERF GSLFSIGLE
